Reconstitution of the allosteric L-lactate dehydrogenase from Lactobacillus casei investigated by hybridization.
The reassociation process of the urea-denatured allosteric L-lactate dehydrogenase from Lactobacillus casei was investigated by hybridization experiments between the reassociating enzymes from L. casei and Lactobacillus curvatus. The quantitatively evaluated hybridization patterns indicate an assembly pathway from the unfolded subunits to the tetrameric state via dimers. The comparison of the kinetics of reassociation and reactivation of the L. casei L-lactate dehydrogenase shows that the tetramer is the only active form.
D000494:Allosteric Regulation; D007700:Kinetics; D007770:L-Lactate Dehydrogenase / Q000378:metabolism*; D007780:Lacticaseibacillus casei / Q000201:enzymology*; D046911:Macromolecular Substances; D008433:Mathematics; D008954:Models, Biological; D055503:Protein Multimerization
D046911:Macromolecular Substances; D007770:L-Lactate Dehydrogenase